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2nlr
From Proteopedia
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STREPTOMYCES LIVIDANS ENDOGLUCANASE (EC: 3.2.1.4) COMPLEX WITH MODIFIED GLUCOSE TRIMER
Overview
Glycoside hydrolases have been classified into over 66 families on the, basis of amino acid sequence. Recently a number of these families have, been grouped into "clans" which share a common fold and catalytic, mechanism [Henrissat, B., and Bairoch, A. (1996) Biochem. J. 316, 695-696]. Glycoside hydrolase Clan GH-C groups family 11 xylanases and, family 12 cellulases, which share the same jellyroll topology, with two, predominantly antiparallel beta-sheets forming a long substrate-binding, cleft, and act with net retention of anomeric configuration. Here we, present the three-dimensional structure of a family 12 endoglucanase, Streptomyces lividans CelB2, in complex with a, 2-deoxy-2-fluorocellotrioside. Atomic resolution (1.2 A) data allow clear, identification of two distinct species in the crystal. One is the, glycosyl-enzyme intermediate, with the mechanism-based inhibitor, covalently linked to the nucleophile Glu 120, and the other a complex with, the reaction product, 2-deoxy-2-fluoro-beta-D-cellotriose. The active site, architecture of the complex provides insight into the double-displacement, mechanism of retaining glycoside hydrolases and also sheds light on the, basis of the differences in specificity between family 12 cellulases and, family 11 xylanases.
About this Structure
2NLR is a Single protein structure of sequence from Streptomyces lividans. Active as Cellulase, with EC number 3.2.1.4 Full crystallographic information is available from OCA.
Reference
The crystal structure of a 2-fluorocellotriosyl complex of the Streptomyces lividans endoglucanase CelB2 at 1.2 A resolution., Sulzenbacher G, Mackenzie LF, Wilson KS, Withers SG, Dupont C, Davies GJ, Biochemistry. 1999 Apr 13;38(15):4826-33. PMID:10200171
Page seeded by OCA on Tue Jan 29 20:55:53 2008
